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Conserved domains on  [gi|1901196470|emb|CAD5330476|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

RING finger protein; RING finger protein 130( domain architecture ID 11613637)

RING finger protein may function as an E3 ubiquitin protein ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin| RING finger protein 130 (RNF130) acts as an E3 ubiquitin-protein ligase that may have a role during the programmed cell death of hematopoietic cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-HC_HAKAI-like cd16508
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Hakai, zinc finger protein 645 ...
 70-119 3.83e-27

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Hakai, zinc finger protein 645 (ZNF645), and similar proteins; Hakai, also known as Casitas B-lineage lymphoma-transforming sequence-like protein 1, RING finger protein 188 (RNF188), or c-Cbl-like protein 1 (CBLL1), is an E3 ubiquitin ligase that disrupts cell-cell contacts in epithelial cells and is upregulated in human colon and gastric adenocarcinomas. It was identified to mediate the posttranslational downregulation of E-cadherin (CDH1), a major component of adherens junctions in epithelial cells and a potent tumor suppressor. It also promotes ubiquitination of several other tyrosine-phosphorylated Src substrates, including cortactin (CTTN) and DOK1. Hakai acts as a homodimer arranged in an anti-parallel configuration with a novel HYB (Hakai pTyr-binding) domain that forms a phosphotyrosine-binding pocket. Each monomer contains a C3HC4-type RING-HC finger and a short pTyr-B domain that incorporates a novel, atypical C2H2-type Zn-finger coordination motif. Both domains are important for dimerization. ZNF645 is a novel testis-specific E3 ubiquitin-protein ligase that plays a role in sperm production and quality control. It has a structure similar to that of the c-Cbl-like protein Hakai. In contrast to Hakai, its HYB domain demonstrates different target specificities. It interacts with v-Src-phosphorylated E-cadherin, but not to cortactin.


:

Pssm-ID: 438171 [Multi-domain]  Cd Length: 51  Bit Score: 101.27  E-value: 3.83e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1901196470  70 HFCVRCDFPIAIYGRLIPCDHAFCLECAR-SDSICYLCDERIQKIQTIKMM 119
Cdd:cd16508     1 HFCDKCDLPIKIYGRMIPCKHVFCLDCARlHDKICPRCDDPVQRIEQCTRG 51
 
Name Accession Description Interval E-value
RING-HC_HAKAI-like cd16508
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Hakai, zinc finger protein 645 ...
 70-119 3.83e-27

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Hakai, zinc finger protein 645 (ZNF645), and similar proteins; Hakai, also known as Casitas B-lineage lymphoma-transforming sequence-like protein 1, RING finger protein 188 (RNF188), or c-Cbl-like protein 1 (CBLL1), is an E3 ubiquitin ligase that disrupts cell-cell contacts in epithelial cells and is upregulated in human colon and gastric adenocarcinomas. It was identified to mediate the posttranslational downregulation of E-cadherin (CDH1), a major component of adherens junctions in epithelial cells and a potent tumor suppressor. It also promotes ubiquitination of several other tyrosine-phosphorylated Src substrates, including cortactin (CTTN) and DOK1. Hakai acts as a homodimer arranged in an anti-parallel configuration with a novel HYB (Hakai pTyr-binding) domain that forms a phosphotyrosine-binding pocket. Each monomer contains a C3HC4-type RING-HC finger and a short pTyr-B domain that incorporates a novel, atypical C2H2-type Zn-finger coordination motif. Both domains are important for dimerization. ZNF645 is a novel testis-specific E3 ubiquitin-protein ligase that plays a role in sperm production and quality control. It has a structure similar to that of the c-Cbl-like protein Hakai. In contrast to Hakai, its HYB domain demonstrates different target specificities. It interacts with v-Src-phosphorylated E-cadherin, but not to cortactin.


Pssm-ID: 438171 [Multi-domain]  Cd Length: 51  Bit Score: 101.27  E-value: 3.83e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1901196470  70 HFCVRCDFPIAIYGRLIPCDHAFCLECAR-SDSICYLCDERIQKIQTIKMM 119
Cdd:cd16508     1 HFCDKCDLPIKIYGRMIPCKHVFCLDCARlHDKICPRCDDPVQRIEQCTRG 51
 
Name Accession Description Interval E-value
RING-HC_HAKAI-like cd16508
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Hakai, zinc finger protein 645 ...
 70-119 3.83e-27

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Hakai, zinc finger protein 645 (ZNF645), and similar proteins; Hakai, also known as Casitas B-lineage lymphoma-transforming sequence-like protein 1, RING finger protein 188 (RNF188), or c-Cbl-like protein 1 (CBLL1), is an E3 ubiquitin ligase that disrupts cell-cell contacts in epithelial cells and is upregulated in human colon and gastric adenocarcinomas. It was identified to mediate the posttranslational downregulation of E-cadherin (CDH1), a major component of adherens junctions in epithelial cells and a potent tumor suppressor. It also promotes ubiquitination of several other tyrosine-phosphorylated Src substrates, including cortactin (CTTN) and DOK1. Hakai acts as a homodimer arranged in an anti-parallel configuration with a novel HYB (Hakai pTyr-binding) domain that forms a phosphotyrosine-binding pocket. Each monomer contains a C3HC4-type RING-HC finger and a short pTyr-B domain that incorporates a novel, atypical C2H2-type Zn-finger coordination motif. Both domains are important for dimerization. ZNF645 is a novel testis-specific E3 ubiquitin-protein ligase that plays a role in sperm production and quality control. It has a structure similar to that of the c-Cbl-like protein Hakai. In contrast to Hakai, its HYB domain demonstrates different target specificities. It interacts with v-Src-phosphorylated E-cadherin, but not to cortactin.


Pssm-ID: 438171 [Multi-domain]  Cd Length: 51  Bit Score: 101.27  E-value: 3.83e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1901196470  70 HFCVRCDFPIAIYGRLIPCDHAFCLECAR-SDSICYLCDERIQKIQTIKMM 119
Cdd:cd16508     1 HFCDKCDLPIKIYGRMIPCKHVFCLDCARlHDKICPRCDDPVQRIEQCTRG 51
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
 72-106 7.39e-03

RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 34.25  E-value: 7.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1901196470  72 CVRCDFPIAIYGRLIPCDHAFCLEC----ARSDSICYLC 106
Cdd:cd23130     3 CPICLDDPEDEAITLPCLHQFCYTCilrwLQTSPTCPLC 41
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
 84-110 8.73e-03

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438228 [Multi-domain]  Cd Length: 43  Bit Score: 33.87  E-value: 8.73e-03
                          10        20
                  ....*....|....*....|....*...
gi 1901196470  84 RLIPCDHA-FCLECARSDSICYLCDERI 110
Cdd:cd16566    16 ELRPCGHSgFCMECALQLETCPLCRQPI 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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